4HTG

Porphobilinogen Deaminase from Arabidopsis Thaliana

Summary for 4HTG

Entry DOI	10.2210/pdb4htg/pdb
Related	1gtk 1pda 3ecr 3eq1
Descriptor	Porphobilinogen deaminase, chloroplastic, 3-[(5Z)-5-{[3-(2-carboxyethyl)-4-(carboxymethyl)-5-methyl-1H-pyrrol-2-yl]methylidene}-4-(carboxymethyl)-2-oxo-2,5-dihydro-1H-pyrrol-3-yl]propanoic acid, ACETATE ION, ... (4 entities in total)
Functional Keywords	type-ii periplasmic binding protein fold, porphyrin binding, tetrapyrrole biosynthesis, porphobilinogen (porphyrin) binding, chloroplast, transferase-transferase inhibitor complex, transferase/transferase inhibitor
Biological source	Arabidopsis thaliana (mouse-ear cress,thale-cress)
Cellular location	Plastid, chloroplast: Q43316
Total number of polymer chains	1
Total formula weight	35151.31
Authors	Roberts, A.,Gill, R.,Hussey, R.J.,Erskine, P.T.,Cooper, J.B.,Wood, S.P.,Chrystal, E.J.T.,Shoolingin-Jordan, P.M. (deposition date: 2012-11-01, release date: 2013-02-27, Last modification date: 2023-09-20)
Primary citation	Roberts, A.,Gill, R.,Hussey, R.J.,Mikolajek, H.,Erskine, P.T.,Cooper, J.B.,Wood, S.P.,Chrystal, E.J.,Shoolingin-Jordan, P.M. Insights into the mechanism of pyrrole polymerization catalysed by porphobilinogen deaminase: high-resolution X-ray studies of the Arabidopsis thaliana enzyme. Acta Crystallogr.,Sect.D, 69:471-485, 2013 Cited by PubMed: 23519422 DOI: 10.1107/S0907444912052134 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.45 Å)

Structure validation